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Towards improved quality of GPCR models by usage of multiple templates and profile-profile comparison.


ABSTRACT:

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G-protein coupled receptors (GPCRs) are targets of nearly one third of the drugs at the current pharmaceutical market. Despite their importance in many cellular processes the crystal structures are available for less than 20 unique GPCRs of the Rhodopsin-like class. Fortunately, even though involved in different signaling cascades, this large group of membrane proteins has preserved a uniform structure comprising seven transmembrane helices that allows quite reliable comparative modeling. Nevertheless, low sequence similarity between the GPCR family members is still a serious obstacle not only in template selection but also in providing theoretical models of acceptable quality. An additional level of difficulty is the prediction of kinks and bulges in transmembrane helic

SUBMITTER: Latek D 

PROVIDER: S-EPMC3585245 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature